PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
25940306-0	2015	Salicylate activates AMPK and synergizes with metformin to reduce the survival of prostate and lung cancer cells ex vivo through inhibition of de novo lipogenesis.	Salicylates	0-10	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	21-25	
28924239-2	2017	Activation of AMPK by salicylate and the thienopyridone A-769662 is critically dependent on phosphorylation of Ser108 in the beta1 regulatory subunit.	Salicylates	22-32	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	14-18	
25940306-2	2015	Salicylate activates the AMP-activated protein kinase (AMPK) by binding at the A-769662 drug binding site on the AMPK beta1-subunit, a mechanism that is distinct from metformin which disrupts the adenylate charge of the cell.	Salicylates	0-10	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	25-53	
25940306-2	2015	Salicylate activates the AMP-activated protein kinase (AMPK) by binding at the A-769662 drug binding site on the AMPK beta1-subunit, a mechanism that is distinct from metformin which disrupts the adenylate charge of the cell.	Salicylates	0-10	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	55-59	
25940306-2	2015	Salicylate activates the AMP-activated protein kinase (AMPK) by binding at the A-769662 drug binding site on the AMPK beta1-subunit, a mechanism that is distinct from metformin which disrupts the adenylate charge of the cell.	Salicylates	0-10	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	113-117	
25940306-6	2015	Salicylate concentrations of 1 mM increased the phosphorylation of ACC and suppressed de novo lipogenesis and these effects were enhanced with the addition of clinical concentrations of metformin (100 muM) and eliminated in mouse embryonic fibroblasts (MEFs) deficient in AMPK beta1.	Salicylates	0-10	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	272-276	
25742316-0	2015	Metformin and salicylate synergistically activate liver AMPK, inhibit lipogenesis and improve insulin sensitivity.	Salicylates	14-24	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	56-60	
25742316-2	2015	Metformin and salicylate both increase AMP-activated protein kinase (AMPK) activity but by distinct mechanisms, with metformin altering cellular adenylate charge (increasing AMP) and salicylate interacting directly at the AMPK beta1 drug-binding site.	Salicylates	14-24	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	39-67	
25742316-2	2015	Metformin and salicylate both increase AMP-activated protein kinase (AMPK) activity but by distinct mechanisms, with metformin altering cellular adenylate charge (increasing AMP) and salicylate interacting directly at the AMPK beta1 drug-binding site.	Salicylates	14-24	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	69-73	
25742316-2	2015	Metformin and salicylate both increase AMP-activated protein kinase (AMPK) activity but by distinct mechanisms, with metformin altering cellular adenylate charge (increasing AMP) and salicylate interacting directly at the AMPK beta1 drug-binding site.	Salicylates	14-24	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	222-226	
25742316-2	2015	Metformin and salicylate both increase AMP-activated protein kinase (AMPK) activity but by distinct mechanisms, with metformin altering cellular adenylate charge (increasing AMP) and salicylate interacting directly at the AMPK beta1 drug-binding site.	Salicylates	183-193	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	222-226	
25742316-4	2015	We find doses of metformin and salicylate used clinically synergistically activate AMPK in vitro and in vivo, resulting in reduced liver lipogenesis, lower liver lipid levels and improved insulin sensitivity in mice.	Salicylates	31-41	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	83-87	
23721051-5	2013	AMPKbeta1- and AMPKbeta2-containing complexes differ in their capacity to be activated by specific drugs (i.e. A769622, salicylate) and also by the ability to undergo post-translational modifications.	Salicylates	120-130	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	0-9	
32519244-6	2020	Moreover, the activity of GSK3beta and the level of Tau phosphorylation (Ser396 and Thr231 sites) were significantly decreased in HEK293 Tau cells transfected by AMPK plasmid or treated with agonists salicylate (SS), but GSK3beta agonists Wortmannin (Wort) could ablate AMPK-mediated Tau dephosphorylation.	Salicylates	200-210	protein kinase AMP-activated non-catalytic subunit beta 1	Homo sapiens	162-166